MX2_BOVIN
ID MX2_BOVIN Reviewed; 710 AA.
AC Q9BDI7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Interferon-induced GTP-binding protein Mx2;
DE AltName: Full=Myxovirus resistance protein 2;
GN Name=MX2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Endometrium;
RA Gordy P.W., Bowen R.A.;
RT "Bos taurus GTP-binding protein (Mx2) mRNA sequence.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND VARIANTS SER-302 AND VAL-354.
RX PubMed=17119954; DOI=10.1007/s00251-006-0167-5;
RA Babiker H.A.E., Nakatsu Y., Yamada K., Yoneda A., Takada A., Ueda J.,
RA Hata H., Watanabe T.;
RT "Bovine and water buffalo Mx2 genes: polymorphism and antiviral activity.";
RL Immunogenetics 59:59-67(2007).
RN [3]
RP REVIEW, AND INDUCTION.
RX PubMed=18062906; DOI=10.1016/j.micinf.2007.09.010;
RA Haller O., Stertz S., Kochs G.;
RT "The Mx GTPase family of interferon-induced antiviral proteins.";
RL Microbes Infect. 9:1636-1643(2007).
CC -!- FUNCTION: Interferon-induced dynamin-like GTPase with antiviral
CC activity against vesicular stomatitis virus (VSV).
CC {ECO:0000269|PubMed:17119954}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- INDUCTION: By type I and type III interferons.
CC {ECO:0000269|PubMed:18062906}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; AF355147; AAK25824.1; -; mRNA.
DR RefSeq; NP_776366.1; NM_173941.2.
DR AlphaFoldDB; Q9BDI7; -.
DR SMR; Q9BDI7; -.
DR STRING; 9913.ENSBTAP00000011146; -.
DR PaxDb; Q9BDI7; -.
DR PRIDE; Q9BDI7; -.
DR GeneID; 280873; -.
DR KEGG; bta:280873; -.
DR CTD; 4600; -.
DR eggNOG; KOG0446; Eukaryota.
DR InParanoid; Q9BDI7; -.
DR OrthoDB; 494748at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Cytoplasm; GTP-binding; Immunity; Innate immunity;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..710
FT /note="Interferon-induced GTP-binding protein Mx2"
FT /id="PRO_0000319957"
FT DOMAIN 112..383
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 619..710
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..129
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 147..149
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 221..224
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 290..293
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 322..325
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT BINDING 122..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 221..225
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 290..293
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VARIANT 302
FT /note="G -> S"
FT /evidence="ECO:0000269|PubMed:17119954"
FT VARIANT 354
FT /note="I -> V"
FT /evidence="ECO:0000269|PubMed:17119954"
SQ SEQUENCE 710 AA; 81452 MW; 83C8FA706B2A0C2B CRC64;
MSMSFRPLKY KRHTQTSTQH HPKQDIYFHQ QPPGPPLGQT MSPPQWQVEE SNPDFLPNNF
NQLNLDPQQP EAKGGQQMSK GPENNLYRKY EEKVRPCIDL IDSLRALGVE QDLALPAIAV
IGDQSSGKSS VLEALSGVAL PRGSGIITRC PLVLKLTKRE CEWTGKITYR NITQQLQNPS
EVEWEIRRAQ NIIAGNGLGI SHELINLEIT SPEVPDLTLI DLPGITRVAV ENQPQDIGLQ
IKALIKKYIQ RQETINLVVV PCNVDIATTE ALSMAQEVDP DGDRTIGILT KPDLVDKGTE
KGVLKVMQNL TYHLKKGYMI VKCRGQQDIT NKLSLAEATR KETMFFETHP YFRILLDEGK
ATVPLLAERL TTELIWHINK SLPLLENQIK EKHQRATEEL QQYGDDIPSD EGDKMFFLIE
KIKVFNEDIG KLIEGEEIVM ETESRLCNKI REEFTSWILI LTTNIEKVKS ILNEEVSKYE
KKYRGKELLG FVNYKTFETV VKHYLGQLID PALKMLQKAM EIVWQTFKDT AKKHFAEFCN
LHQTVQNKIE DIKTKQMAEA ANLIQLQFRM EKLVFCQDQI YGVVLNKVRE DIFNSMGKAS
ETPQSKQPFL NDQSSISSIV EIGVHLNAYF METSKRLANQ IPFIIQYFML QENGDKVQKA
MMQLLQDTQH YSWLLQEQSD TATKRKFLKE KIFRLTQAQQ ALYEFPHFKG
